PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7061105-3 1982 Platelet activation induced by H-CRP was sensitive to the presence of EDTA and dibucaine, required metabolic energy and was inhibited by increased levels of cAMP. Cyclic AMP 157-161 C-reactive protein Homo sapiens 31-36 2837757-1 1988 Four cAMP-independent receptor protein mutants (designated CRP* mutants) isolated previously are able to activate in vivo gene transcription in the absence of cAMP and their activity can be enhanced by cAMP or cGMP. Cyclic AMP 5-9 C-reactive protein Homo sapiens 59-63 2837757-1 1988 Four cAMP-independent receptor protein mutants (designated CRP* mutants) isolated previously are able to activate in vivo gene transcription in the absence of cAMP and their activity can be enhanced by cAMP or cGMP. Cyclic AMP 159-163 C-reactive protein Homo sapiens 59-63 2837757-1 1988 Four cAMP-independent receptor protein mutants (designated CRP* mutants) isolated previously are able to activate in vivo gene transcription in the absence of cAMP and their activity can be enhanced by cAMP or cGMP. Cyclic AMP 159-163 C-reactive protein Homo sapiens 59-63 2837757-4 1988 Binding of wild-type CRP to its site on the lac promoter and activation of abortive initiation by RNA polymerase on this promoter are effected by cAMP but not by cGMP. Cyclic AMP 146-150 C-reactive protein Homo sapiens 21-24 2837757-5 1988 CRP*598 can activate lacP+-directed abortive initiation in the presence of cAMP and less efficiently in the presence of cGMP or in the absence of cyclic nucleotide. Cyclic AMP 75-79 C-reactive protein Homo sapiens 0-3 2837757-6 1988 DNase I protection ("foot-printing") indicates that cAMP-CRP* binds to its site on the lac promoter whereas unliganded CRP* and cGMP-CRP* form a stable complex with the [32P]lacP+ fragment only in the presence of RNA polymerase, showing cooperative binding of two heterologous proteins. Cyclic AMP 52-56 C-reactive protein Homo sapiens 57-60 2837757-6 1988 DNase I protection ("foot-printing") indicates that cAMP-CRP* binds to its site on the lac promoter whereas unliganded CRP* and cGMP-CRP* form a stable complex with the [32P]lacP+ fragment only in the presence of RNA polymerase, showing cooperative binding of two heterologous proteins. Cyclic AMP 52-56 C-reactive protein Homo sapiens 57-61 2837757-9 1988 In contrast, the weakly active unliganded CRP*598 can be shifted to a functional state not only by cAMP but also by cGMP and RNA polymerase. Cyclic AMP 99-103 C-reactive protein Homo sapiens 42-45 3028793-3 1987 Correlation between modulation of cell function, at least at relatively high CRP concentrations (greater than 50 micrograms/ml) and an increase in the intracellular level of cAMP is suggested. Cyclic AMP 174-178 C-reactive protein Homo sapiens 77-80 3045325-9 1988 When the known recognition sites for CRP are ranked according to predicted binding affinities, we find that the ranking is consistent with the hypothesis that the level of function of these sites parallels their fractional saturation with CRP-cAMP under in-vivo conditions. Cyclic AMP 243-247 C-reactive protein Homo sapiens 37-40 3045325-9 1988 When the known recognition sites for CRP are ranked according to predicted binding affinities, we find that the ranking is consistent with the hypothesis that the level of function of these sites parallels their fractional saturation with CRP-cAMP under in-vivo conditions. Cyclic AMP 243-247 C-reactive protein Homo sapiens 239-242 2425359-1 1986 Expression of the crp gene is negatively autoregulated by the complex of cyclic AMP and its receptor protein (cAMP-CRP). Cyclic AMP 110-114 C-reactive protein Homo sapiens 18-21 2425359-1 1986 Expression of the crp gene is negatively autoregulated by the complex of cyclic AMP and its receptor protein (cAMP-CRP). Cyclic AMP 110-114 C-reactive protein Homo sapiens 115-118 2425359-2 1986 We find a second promoter in this region that is strongly activated in vitro and in vivo by cAMP-CRP. Cyclic AMP 92-96 C-reactive protein Homo sapiens 97-100 2425359-5 1986 cAMP-CRP does not block crp expression if the new promoter is altered so that divergent RNA cannot be made. Cyclic AMP 0-4 C-reactive protein Homo sapiens 5-8 6396081-2 1984 Binding of CRP to a 62-bp fragment containing the major site leads to an increase of the rotation time constant from 0.33 to 0.43 microseconds; addition of cAMP to the complex induces a decrease to 0.25 microseconds. Cyclic AMP 156-160 C-reactive protein Homo sapiens 11-14 6396081-7 1984 The rotation time constants together with the dichroism amplitudes indicate that binding of CRP to specific sites in the presence of cAMP leads to the formation of compact structures, which are consistent with bending of DNA helices. Cyclic AMP 133-137 C-reactive protein Homo sapiens 92-95 6316274-1 1983 We have determined the stoichiometry of CRP binding to various DNA fragments carrying the lac, malT or gal promoters in the presence of cAMP, using a gel electrophoresis method. Cyclic AMP 136-140 C-reactive protein Homo sapiens 40-43 6316274-4 1983 Direct binding analysis and competition experiments performed at 200 microM cAMP allow us to measure the affinity of CRP for these different sites and to correlate them with variations in the consensus sequences, already proposed. Cyclic AMP 76-80 C-reactive protein Homo sapiens 117-120 6316274-7 1983 Conversely, we have studied, at constant CRP concentrations, the cAMP levels required to obtain half maximal binding to a particular DNA site : the required cAMP level increases inversely as the affinity for CRP. Cyclic AMP 65-69 C-reactive protein Homo sapiens 208-211 6316274-7 1983 Conversely, we have studied, at constant CRP concentrations, the cAMP levels required to obtain half maximal binding to a particular DNA site : the required cAMP level increases inversely as the affinity for CRP. Cyclic AMP 157-161 C-reactive protein Homo sapiens 208-211 70475-2 1977 The role of cAMP, contractile elements, and prostaglandin metabolism in CRP-induced inhibition of platelet aggregation and secretion. Cyclic AMP 12-16 C-reactive protein Homo sapiens 72-75 6269081-1 1981 We have demonstrated in vitro the existence on the plasmid pBR322 of a promoter signal that is strictly dependent on cAMP and its receptor protein CRP. Cyclic AMP 117-121 C-reactive protein Homo sapiens 147-150 32528421-0 2020 The Regulation of Bacterial Biofilm Formation by cAMP-CRP: A Mini-Review. Cyclic AMP 49-53 C-reactive protein Homo sapiens 54-57 33203750-7 2020 The loss of nqrA or nqrF led to the decrease of membrane potential, ATPase activity, and then ATP and cyclic AMP (cAMP), which reduced the cAMP/CRP (cAMP receptor protein) complex. Cyclic AMP 102-112 C-reactive protein Homo sapiens 144-147 33203750-7 2020 The loss of nqrA or nqrF led to the decrease of membrane potential, ATPase activity, and then ATP and cyclic AMP (cAMP), which reduced the cAMP/CRP (cAMP receptor protein) complex. Cyclic AMP 114-118 C-reactive protein Homo sapiens 144-147 33203750-7 2020 The loss of nqrA or nqrF led to the decrease of membrane potential, ATPase activity, and then ATP and cyclic AMP (cAMP), which reduced the cAMP/CRP (cAMP receptor protein) complex. Cyclic AMP 139-143 C-reactive protein Homo sapiens 144-147 33203750-7 2020 The loss of nqrA or nqrF led to the decrease of membrane potential, ATPase activity, and then ATP and cyclic AMP (cAMP), which reduced the cAMP/CRP (cAMP receptor protein) complex. Cyclic AMP 139-143 C-reactive protein Homo sapiens 144-147 33203750-8 2020 The reduced cAMP/CRP complex promoted l-alanine catabolism and inhibited l-alanine anabolism, causing reduced levels of alanine. Cyclic AMP 12-16 C-reactive protein Homo sapiens 17-20 33203750-10 2020 Our results suggest a novel mechanism by which the Na+-NQR system regulates antibiotic resistance via l-alanine metabolism in a cAMP/CRP complex-dependent manner.IMPORTANCE The Na+-NQR complex functions as a unique redox-driven sodium pump, generating membrane potential directly. Cyclic AMP 128-132 C-reactive protein Homo sapiens 133-136 33203750-13 2020 It proceeds by ATP and then cAMP/CRP regulon, which inhibits l-alanine catabolism and promotes l-alanine anabolism. Cyclic AMP 28-32 C-reactive protein Homo sapiens 33-36 33203750-16 2020 These findings suggest a novel mechanism by which the Na+-NQR system regulates antibiotic resistance via l-alanine metabolism in a cAMP/CRP complex-dependent manner. Cyclic AMP 131-135 C-reactive protein Homo sapiens 136-139 32528421-5 2020 Although the underlying mechanisms of biofilm formation mediated by cAMP-CRP have been well-investigated in several bacteria, the regulatory pathways of cAMP-CRP are still poorly understood compared to those of c-di-GMP. Cyclic AMP 68-72 C-reactive protein Homo sapiens 73-76 32528421-8 2020 This mini-review provides an overview of the cAMP-CRP-regulated pathways involved in biofilm formation in some bacteria. Cyclic AMP 45-49 C-reactive protein Homo sapiens 50-53 24914983-1 2014 The prokaryotic global transcription factor CRP has been considered to be an ideal model for in-depth study of both the allostery of the protein and the differential utilization of the homologous cyclic nucleotide second messengers cAMP and cGMP. Cyclic AMP 232-236 C-reactive protein Homo sapiens 44-47 30256816-3 2018 We first consider the allosteric transition resulting from cyclic-AMP binding to CRP, then analyze how CRP binds to its operator, and finally investigate the ability of CRP to activate gene expression. Cyclic AMP 59-69 C-reactive protein Homo sapiens 81-84 28245055-4 2017 Therefore, our findings suggest that dissociation of the CDD may be critically involved in cAMP-induced allosteric activation of CRP. Cyclic AMP 91-95 C-reactive protein Homo sapiens 129-132 26436683-11 2015 CONCLUSIONS: The 6-week camp intervention resulted in reductions in CRP and leptin. Cyclic AMP 24-28 C-reactive protein Homo sapiens 68-71 24914983-2 2014 Here, atomic details from the crystal structures of two inactive CRP species, an apo form and a cGMP-bound form, in comparison with a known active conformation, the cAMP-CRP complex, provide macroscopic and microscopic insights into CRP allostery, which is coupled to specific discrimination between the two effectors. Cyclic AMP 165-169 C-reactive protein Homo sapiens 65-68 24914983-2 2014 Here, atomic details from the crystal structures of two inactive CRP species, an apo form and a cGMP-bound form, in comparison with a known active conformation, the cAMP-CRP complex, provide macroscopic and microscopic insights into CRP allostery, which is coupled to specific discrimination between the two effectors. Cyclic AMP 165-169 C-reactive protein Homo sapiens 170-173 24914983-2 2014 Here, atomic details from the crystal structures of two inactive CRP species, an apo form and a cGMP-bound form, in comparison with a known active conformation, the cAMP-CRP complex, provide macroscopic and microscopic insights into CRP allostery, which is coupled to specific discrimination between the two effectors. Cyclic AMP 165-169 C-reactive protein Homo sapiens 170-173 21779799-1 2012 Lac operon transcription activation through CRP dimer depends on cAMP second messenger. Cyclic AMP 65-69 C-reactive protein Homo sapiens 44-47 23115037-8 2013 We conclude that balanced input from many cAMP-CRP-responsive elements, including RpoS, is critical to the ability of UPEC to handle the nutrient limitations and severe environmental stresses present within the mammalian urinary tract. Cyclic AMP 42-46 C-reactive protein Homo sapiens 47-50 21779799-3 2012 Cyclic AMP ligand binding brings CRP dimer to an active state via conformational changes. Cyclic AMP 0-10 C-reactive protein Homo sapiens 33-36 21779799-7 2012 CRP monomer exchange accelerates in the presence of non specific DNA whereas the exchange is inhibited in the presence of specific DNA and cAMP ligand. Cyclic AMP 139-143 C-reactive protein Homo sapiens 0-3 21779799-9 2012 Cyclic AMP forms a single molecule from two monomers and addition of specific DNA further stabilizes CRP dimer and decreases monomer exchange. Cyclic AMP 0-10 C-reactive protein Homo sapiens 101-104 21779799-10 2012 On the other hand, addition of non specific DNA increases CRP monomer exchange and may explain the mechanism of CRP monomer removal and dissociation of CRP dimer:cAMP:DNA complex. Cyclic AMP 162-166 C-reactive protein Homo sapiens 58-61 21779799-10 2012 On the other hand, addition of non specific DNA increases CRP monomer exchange and may explain the mechanism of CRP monomer removal and dissociation of CRP dimer:cAMP:DNA complex. Cyclic AMP 162-166 C-reactive protein Homo sapiens 112-115 21779799-10 2012 On the other hand, addition of non specific DNA increases CRP monomer exchange and may explain the mechanism of CRP monomer removal and dissociation of CRP dimer:cAMP:DNA complex. Cyclic AMP 162-166 C-reactive protein Homo sapiens 112-115 19359484-1 2009 The cAMP-mediated allosteric transition in the catabolite activator protein (CAP; also known as the cAMP receptor protein, CRP) is a textbook example of modulation of DNA-binding activity by small-molecule binding. Cyclic AMP 4-8 C-reactive protein Homo sapiens 123-126 19075028-9 2009 Since glucose inhibits the activity of CRP by suppressing the pathogen"s synthesis of cyclic AMP (cAMP), the concentration of glucose in the lumen of the small intestine may determine which enterotoxin is maximally expressed. Cyclic AMP 86-96 C-reactive protein Homo sapiens 39-42 19075028-9 2009 Since glucose inhibits the activity of CRP by suppressing the pathogen"s synthesis of cyclic AMP (cAMP), the concentration of glucose in the lumen of the small intestine may determine which enterotoxin is maximally expressed. Cyclic AMP 98-102 C-reactive protein Homo sapiens 39-42 18084042-4 2008 The results indicated that apo-CRP possesses characteristic modules of interdomain interaction that are properly organized to suppress activity and to sense and transfer the cAMP binding signals. Cyclic AMP 174-178 C-reactive protein Homo sapiens 31-34 18695981-5 2008 In RA patients, SF cAMP level showed negative correlation with Disease Activity Score including a 28-joint count and S CRP, ESR and SF IL-18 level. Cyclic AMP 19-23 C-reactive protein Homo sapiens 119-122 17942113-9 2007 In the present study, CRP-mediated inhibition of GTPCH1 activity was reversed by pretreatment with cAMP analogues. Cyclic AMP 99-103 C-reactive protein Homo sapiens 22-25 16586530-1 2006 The ab initio fragment molecular orbital (FMO) calculations were performed for the cAMP receptor protein (CRP) complexed with a cAMP and DNA duplex to elucidate their sequence-specific binding and the stability of the DNA duplex, as determined by analysis of their inter- and intramolecular interactions. Cyclic AMP 83-87 C-reactive protein Homo sapiens 106-109 16917108-0 2006 C-reactive protein decreases interleukin-10 secretion in activated human monocyte-derived macrophages via inhibition of cyclic AMP production. Cyclic AMP 120-130 C-reactive protein Homo sapiens 0-18 16917108-8 2006 CRP significantly decreased intracellular cAMP, phospho-cAMP response element binding protein (pCREB), and adenyl cyclase activity. Cyclic AMP 42-46 C-reactive protein Homo sapiens 0-3 16917108-8 2006 CRP significantly decreased intracellular cAMP, phospho-cAMP response element binding protein (pCREB), and adenyl cyclase activity. Cyclic AMP 56-60 C-reactive protein Homo sapiens 0-3 16917108-9 2006 cAMP agonists reversed CRP-mediated IL-10 inhibition. Cyclic AMP 0-4 C-reactive protein Homo sapiens 23-26 16401068-6 2006 The Forster resonance energy transfer method has been used to study the distance changes, induced by binding of cAMP, between Trp85 (fluorescence donor) and Cys178-AEDANS (fluorescence acceptor) in the CRP structure. Cyclic AMP 112-116 C-reactive protein Homo sapiens 202-205 14638413-7 2003 The Crp-Fnr regulators stand out in responding to a broad spectrum of intracellular and exogenous signals such as cAMP, anoxia, the redox state, oxidative and nitrosative stress, nitric oxide, carbon monoxide, 2-oxoglutarate, or temperature. Cyclic AMP 114-118 C-reactive protein Homo sapiens 4-7 12667067-0 2003 Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery. Cyclic AMP 29-33 C-reactive protein Homo sapiens 15-18 12667067-8 2003 The binding constants that drive the formation of the WT and L124I CRP-cAMP complexes deviated by not more than a factor of 1.5. Cyclic AMP 71-75 C-reactive protein Homo sapiens 67-70 12667067-10 2003 The data indicate that the van der Waals volume and/or the hyrophobicity of the L124 side chain are important determinants of CRP cAMP binding properties and affect, either directly or indirectly, cAMP-mediated conformation changes in CRP. Cyclic AMP 130-134 C-reactive protein Homo sapiens 126-129 12667067-10 2003 The data indicate that the van der Waals volume and/or the hyrophobicity of the L124 side chain are important determinants of CRP cAMP binding properties and affect, either directly or indirectly, cAMP-mediated conformation changes in CRP. Cyclic AMP 130-134 C-reactive protein Homo sapiens 235-238 12667067-10 2003 The data indicate that the van der Waals volume and/or the hyrophobicity of the L124 side chain are important determinants of CRP cAMP binding properties and affect, either directly or indirectly, cAMP-mediated conformation changes in CRP. Cyclic AMP 197-201 C-reactive protein Homo sapiens 126-129 12667067-10 2003 The data indicate that the van der Waals volume and/or the hyrophobicity of the L124 side chain are important determinants of CRP cAMP binding properties and affect, either directly or indirectly, cAMP-mediated conformation changes in CRP. Cyclic AMP 197-201 C-reactive protein Homo sapiens 235-238 12590582-1 2003 The interaction between CRP, T127L, S128A, and CRP and RNA polymerase bound to a 104 bp synthetic promoter were determined by ITC at 298 K and ranges from a deltaG(b) degrees = 1.4 +/- 0.8 kJ mol(-)(1) (cAMP-ligated S128A) to 4.5 +/- 0.3 kJ mol(-)(1) (cAMP-ligated double mutant CRP) with endothermicities that range from 4 +/- 3 kJ mol(-)(1) (cAMP-ligated CRP) to 47 +/- 8 kJ mol(-)(1) (cGMP-ligated T127L). Cyclic AMP 203-207 C-reactive protein Homo sapiens 24-27 12590582-1 2003 The interaction between CRP, T127L, S128A, and CRP and RNA polymerase bound to a 104 bp synthetic promoter were determined by ITC at 298 K and ranges from a deltaG(b) degrees = 1.4 +/- 0.8 kJ mol(-)(1) (cAMP-ligated S128A) to 4.5 +/- 0.3 kJ mol(-)(1) (cAMP-ligated double mutant CRP) with endothermicities that range from 4 +/- 3 kJ mol(-)(1) (cAMP-ligated CRP) to 47 +/- 8 kJ mol(-)(1) (cGMP-ligated T127L). Cyclic AMP 203-207 C-reactive protein Homo sapiens 47-50 12590582-1 2003 The interaction between CRP, T127L, S128A, and CRP and RNA polymerase bound to a 104 bp synthetic promoter were determined by ITC at 298 K and ranges from a deltaG(b) degrees = 1.4 +/- 0.8 kJ mol(-)(1) (cAMP-ligated S128A) to 4.5 +/- 0.3 kJ mol(-)(1) (cAMP-ligated double mutant CRP) with endothermicities that range from 4 +/- 3 kJ mol(-)(1) (cAMP-ligated CRP) to 47 +/- 8 kJ mol(-)(1) (cGMP-ligated T127L). Cyclic AMP 203-207 C-reactive protein Homo sapiens 47-50 12590582-1 2003 The interaction between CRP, T127L, S128A, and CRP and RNA polymerase bound to a 104 bp synthetic promoter were determined by ITC at 298 K and ranges from a deltaG(b) degrees = 1.4 +/- 0.8 kJ mol(-)(1) (cAMP-ligated S128A) to 4.5 +/- 0.3 kJ mol(-)(1) (cAMP-ligated double mutant CRP) with endothermicities that range from 4 +/- 3 kJ mol(-)(1) (cAMP-ligated CRP) to 47 +/- 8 kJ mol(-)(1) (cGMP-ligated T127L). Cyclic AMP 203-207 C-reactive protein Homo sapiens 47-50 12590582-1 2003 The interaction between CRP, T127L, S128A, and CRP and RNA polymerase bound to a 104 bp synthetic promoter were determined by ITC at 298 K and ranges from a deltaG(b) degrees = 1.4 +/- 0.8 kJ mol(-)(1) (cAMP-ligated S128A) to 4.5 +/- 0.3 kJ mol(-)(1) (cAMP-ligated double mutant CRP) with endothermicities that range from 4 +/- 3 kJ mol(-)(1) (cAMP-ligated CRP) to 47 +/- 8 kJ mol(-)(1) (cGMP-ligated T127L). Cyclic AMP 252-256 C-reactive protein Homo sapiens 24-27 12590582-1 2003 The interaction between CRP, T127L, S128A, and CRP and RNA polymerase bound to a 104 bp synthetic promoter were determined by ITC at 298 K and ranges from a deltaG(b) degrees = 1.4 +/- 0.8 kJ mol(-)(1) (cAMP-ligated S128A) to 4.5 +/- 0.3 kJ mol(-)(1) (cAMP-ligated double mutant CRP) with endothermicities that range from 4 +/- 3 kJ mol(-)(1) (cAMP-ligated CRP) to 47 +/- 8 kJ mol(-)(1) (cGMP-ligated T127L). Cyclic AMP 252-256 C-reactive protein Homo sapiens 47-50 12590582-1 2003 The interaction between CRP, T127L, S128A, and CRP and RNA polymerase bound to a 104 bp synthetic promoter were determined by ITC at 298 K and ranges from a deltaG(b) degrees = 1.4 +/- 0.8 kJ mol(-)(1) (cAMP-ligated S128A) to 4.5 +/- 0.3 kJ mol(-)(1) (cAMP-ligated double mutant CRP) with endothermicities that range from 4 +/- 3 kJ mol(-)(1) (cAMP-ligated CRP) to 47 +/- 8 kJ mol(-)(1) (cGMP-ligated T127L). Cyclic AMP 252-256 C-reactive protein Homo sapiens 47-50 12590582-1 2003 The interaction between CRP, T127L, S128A, and CRP and RNA polymerase bound to a 104 bp synthetic promoter were determined by ITC at 298 K and ranges from a deltaG(b) degrees = 1.4 +/- 0.8 kJ mol(-)(1) (cAMP-ligated S128A) to 4.5 +/- 0.3 kJ mol(-)(1) (cAMP-ligated double mutant CRP) with endothermicities that range from 4 +/- 3 kJ mol(-)(1) (cAMP-ligated CRP) to 47 +/- 8 kJ mol(-)(1) (cGMP-ligated T127L). Cyclic AMP 252-256 C-reactive protein Homo sapiens 47-50 12590582-1 2003 The interaction between CRP, T127L, S128A, and CRP and RNA polymerase bound to a 104 bp synthetic promoter were determined by ITC at 298 K and ranges from a deltaG(b) degrees = 1.4 +/- 0.8 kJ mol(-)(1) (cAMP-ligated S128A) to 4.5 +/- 0.3 kJ mol(-)(1) (cAMP-ligated double mutant CRP) with endothermicities that range from 4 +/- 3 kJ mol(-)(1) (cAMP-ligated CRP) to 47 +/- 8 kJ mol(-)(1) (cGMP-ligated T127L). Cyclic AMP 252-256 C-reactive protein Homo sapiens 24-27 12590582-1 2003 The interaction between CRP, T127L, S128A, and CRP and RNA polymerase bound to a 104 bp synthetic promoter were determined by ITC at 298 K and ranges from a deltaG(b) degrees = 1.4 +/- 0.8 kJ mol(-)(1) (cAMP-ligated S128A) to 4.5 +/- 0.3 kJ mol(-)(1) (cAMP-ligated double mutant CRP) with endothermicities that range from 4 +/- 3 kJ mol(-)(1) (cAMP-ligated CRP) to 47 +/- 8 kJ mol(-)(1) (cGMP-ligated T127L). Cyclic AMP 252-256 C-reactive protein Homo sapiens 47-50 12590582-1 2003 The interaction between CRP, T127L, S128A, and CRP and RNA polymerase bound to a 104 bp synthetic promoter were determined by ITC at 298 K and ranges from a deltaG(b) degrees = 1.4 +/- 0.8 kJ mol(-)(1) (cAMP-ligated S128A) to 4.5 +/- 0.3 kJ mol(-)(1) (cAMP-ligated double mutant CRP) with endothermicities that range from 4 +/- 3 kJ mol(-)(1) (cAMP-ligated CRP) to 47 +/- 8 kJ mol(-)(1) (cGMP-ligated T127L). Cyclic AMP 252-256 C-reactive protein Homo sapiens 47-50 12590582-1 2003 The interaction between CRP, T127L, S128A, and CRP and RNA polymerase bound to a 104 bp synthetic promoter were determined by ITC at 298 K and ranges from a deltaG(b) degrees = 1.4 +/- 0.8 kJ mol(-)(1) (cAMP-ligated S128A) to 4.5 +/- 0.3 kJ mol(-)(1) (cAMP-ligated double mutant CRP) with endothermicities that range from 4 +/- 3 kJ mol(-)(1) (cAMP-ligated CRP) to 47 +/- 8 kJ mol(-)(1) (cGMP-ligated T127L). Cyclic AMP 252-256 C-reactive protein Homo sapiens 47-50 12590582-2 2003 The interaction is, thus, entropically driven, exhibits enthalpy-entropy compensation, and increases the binding affinity of the RNA polymerase to the promoter by factors ranging from 1.7 +/- 0.1 (cAMP-ligated S128A) to 6.1 +/- 0.1 (cAMP-ligated CRP). Cyclic AMP 197-201 C-reactive protein Homo sapiens 246-249 12590582-2 2003 The interaction is, thus, entropically driven, exhibits enthalpy-entropy compensation, and increases the binding affinity of the RNA polymerase to the promoter by factors ranging from 1.7 +/- 0.1 (cAMP-ligated S128A) to 6.1 +/- 0.1 (cAMP-ligated CRP). Cyclic AMP 233-237 C-reactive protein Homo sapiens 246-249 12667067-0 2003 Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery. Cyclic AMP 29-33 C-reactive protein Homo sapiens 42-45 12667067-0 2003 Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery. Cyclic AMP 29-33 C-reactive protein Homo sapiens 42-45 12667067-0 2003 Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery. Cyclic AMP 46-50 C-reactive protein Homo sapiens 15-18 12667067-0 2003 Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery. Cyclic AMP 46-50 C-reactive protein Homo sapiens 42-45 12667067-0 2003 Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery. Cyclic AMP 46-50 C-reactive protein Homo sapiens 42-45 12667067-0 2003 Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery. Cyclic AMP 46-50 C-reactive protein Homo sapiens 15-18 12667067-0 2003 Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery. Cyclic AMP 46-50 C-reactive protein Homo sapiens 42-45 12667067-0 2003 Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery. Cyclic AMP 46-50 C-reactive protein Homo sapiens 42-45 12667067-4 2003 Wild-type (WT) apo-CRP is a 47 kDa protease-resistant dimer composed of identical subunits that exhibits a biphasic isotherm in cAMP titration studies. Cyclic AMP 128-132 C-reactive protein Homo sapiens 19-22 12667067-5 2003 The WT CRP-cAMP complex is a protease-sensitive dimer degraded by protease to a dimer core that ranges between 26.5 and 30.5 kDa. Cyclic AMP 11-15 C-reactive protein Homo sapiens 7-10 12667067-7 2003 Differences in the affinity of the position 124 CRP variants for cAMP were observed. Cyclic AMP 65-69 C-reactive protein Homo sapiens 48-51 11781328-1 2002 Cyclic AMP receptor protein (CRP) is a homodimeric protein, which is activated by cAMP binding to function as a transcriptional regulator of many genes in prokaryotes. Cyclic AMP 82-86 C-reactive protein Homo sapiens 0-27 11781328-1 2002 Cyclic AMP receptor protein (CRP) is a homodimeric protein, which is activated by cAMP binding to function as a transcriptional regulator of many genes in prokaryotes. Cyclic AMP 82-86 C-reactive protein Homo sapiens 29-32 11781328-2 2002 Until now, the actual number of cAMP molecules that can be bound by CRP in solution has been ambiguous. Cyclic AMP 32-36 C-reactive protein Homo sapiens 68-71 11781328-6 2002 Altogether, the results not only established for the first time that CRP possesses two cyclic AMP-binding sites in each monomer, even in a solution without DNA, but also suggest that the syn-cAMP binding sites of the CRP dimer can be formed by an allosteric conformational change of the protein upon the binding of two anti-cAMPs at the N-terminal domain. Cyclic AMP 87-97 C-reactive protein Homo sapiens 69-72 11781328-6 2002 Altogether, the results not only established for the first time that CRP possesses two cyclic AMP-binding sites in each monomer, even in a solution without DNA, but also suggest that the syn-cAMP binding sites of the CRP dimer can be formed by an allosteric conformational change of the protein upon the binding of two anti-cAMPs at the N-terminal domain. Cyclic AMP 87-97 C-reactive protein Homo sapiens 217-220 11781328-6 2002 Altogether, the results not only established for the first time that CRP possesses two cyclic AMP-binding sites in each monomer, even in a solution without DNA, but also suggest that the syn-cAMP binding sites of the CRP dimer can be formed by an allosteric conformational change of the protein upon the binding of two anti-cAMPs at the N-terminal domain. Cyclic AMP 191-195 C-reactive protein Homo sapiens 69-72 11781328-6 2002 Altogether, the results not only established for the first time that CRP possesses two cyclic AMP-binding sites in each monomer, even in a solution without DNA, but also suggest that the syn-cAMP binding sites of the CRP dimer can be formed by an allosteric conformational change of the protein upon the binding of two anti-cAMPs at the N-terminal domain. Cyclic AMP 191-195 C-reactive protein Homo sapiens 217-220 11781328-7 2002 In addition, a residue-specific inspection of the spectral changes provides some new structural information about the cAMP-induced allosteric activation of CRP. Cyclic AMP 118-122 C-reactive protein Homo sapiens 156-159 10449529-10 1999 On monocytic cell lines, treatment with Bt(2)cAMP increased FcgammaRII expression and enhanced CRP binding. Cyclic AMP 45-49 C-reactive protein Homo sapiens 95-98 11446515-5 2001 The cyclic AMP-CRP complex was shown to stimulate transcription from Pmcc: the absence of CRP or cAMP in crp or cya mutant cells strongly decreased the level of P(mcc)-lac expression. Cyclic AMP 4-14 C-reactive protein Homo sapiens 15-18 11446515-5 2001 The cyclic AMP-CRP complex was shown to stimulate transcription from Pmcc: the absence of CRP or cAMP in crp or cya mutant cells strongly decreased the level of P(mcc)-lac expression. Cyclic AMP 4-14 C-reactive protein Homo sapiens 90-93 11446515-5 2001 The cyclic AMP-CRP complex was shown to stimulate transcription from Pmcc: the absence of CRP or cAMP in crp or cya mutant cells strongly decreased the level of P(mcc)-lac expression. Cyclic AMP 4-14 C-reactive protein Homo sapiens 105-108 11446515-5 2001 The cyclic AMP-CRP complex was shown to stimulate transcription from Pmcc: the absence of CRP or cAMP in crp or cya mutant cells strongly decreased the level of P(mcc)-lac expression. Cyclic AMP 97-101 C-reactive protein Homo sapiens 15-18 11446515-5 2001 The cyclic AMP-CRP complex was shown to stimulate transcription from Pmcc: the absence of CRP or cAMP in crp or cya mutant cells strongly decreased the level of P(mcc)-lac expression. Cyclic AMP 97-101 C-reactive protein Homo sapiens 105-108 11124966-13 2001 94, 2843-2847), imply that the cAMP-ligated CRP* structure is closer to the conformation of the allosterically activated structure than cAMP-ligated CRP. Cyclic AMP 31-35 C-reactive protein Homo sapiens 44-48 11124966-13 2001 94, 2843-2847), imply that the cAMP-ligated CRP* structure is closer to the conformation of the allosterically activated structure than cAMP-ligated CRP. Cyclic AMP 31-35 C-reactive protein Homo sapiens 44-47 11124966-14 2001 This may be induced by the unique flexibility at Ala(128) and/or by the bound syn-cAMP in the hinge region of CRP*. Cyclic AMP 82-86 C-reactive protein Homo sapiens 110-114 11076538-2 2000 CRP is allosterically activated by cyclic AMP and binds to specific DNA sites. Cyclic AMP 35-45 C-reactive protein Homo sapiens 0-3 11076538-7 2000 This secondary structure of apo-CRP was compared with the known structure of cyclic AMP-bound CRP. Cyclic AMP 77-87 C-reactive protein Homo sapiens 32-35 11076538-7 2000 This secondary structure of apo-CRP was compared with the known structure of cyclic AMP-bound CRP. Cyclic AMP 77-87 C-reactive protein Homo sapiens 94-97 11076538-8 2000 The results suggest that the allosteric conformational change of CRP caused by cyclic AMP binding involves subunit realignment and domain rearrangement, resulting in the exposure of helix F onto the surface of the protein. Cyclic AMP 79-89 C-reactive protein Homo sapiens 65-68 11076538-9 2000 Additionally, the results of the one-dimensional [(13)C]carbonyl NMR experiments show that the conformational change of CRP caused by the binding of cyclic GMP, an analogue of cyclic AMP, is different from that caused by cyclic AMP binding. Cyclic AMP 176-186 C-reactive protein Homo sapiens 120-123 11076538-9 2000 Additionally, the results of the one-dimensional [(13)C]carbonyl NMR experiments show that the conformational change of CRP caused by the binding of cyclic GMP, an analogue of cyclic AMP, is different from that caused by cyclic AMP binding. Cyclic AMP 221-231 C-reactive protein Homo sapiens 120-123 11979597-1 2002 Cyclic AMP (cAMP) receptor protein (CRP) forms 1:1 and 1:2 complexes with cAMP, and the former complex is considered to be the most active form of CRP in binding to specific DNA sequences and in modulating gene transcription by RNA polymerases. Cyclic AMP 12-16 C-reactive protein Homo sapiens 36-39 11979597-1 2002 Cyclic AMP (cAMP) receptor protein (CRP) forms 1:1 and 1:2 complexes with cAMP, and the former complex is considered to be the most active form of CRP in binding to specific DNA sequences and in modulating gene transcription by RNA polymerases. Cyclic AMP 12-16 C-reactive protein Homo sapiens 147-150 11979597-2 2002 We examine the cAMP binding modes and structural changes of CRP upon cAMP binding by UV resonance Raman spectroscopy. Cyclic AMP 69-73 C-reactive protein Homo sapiens 60-63 11979597-3 2002 The Raman spectra of CRP-(cAMP)(1) and CRP-(cAMP)(2) extracted from those of CRP-cAMP mixtures at varied mixing ratios clearly show that the hydrogen bonding state and the conformation of cAMP in both complexes in solution are very similar to those found in the X-ray crystal structure of CRP-(cAMP)(2), which is evidence that the cAMP binding mode does not differ between the two complexes. Cyclic AMP 26-30 C-reactive protein Homo sapiens 21-24 11979597-3 2002 The Raman spectra of CRP-(cAMP)(1) and CRP-(cAMP)(2) extracted from those of CRP-cAMP mixtures at varied mixing ratios clearly show that the hydrogen bonding state and the conformation of cAMP in both complexes in solution are very similar to those found in the X-ray crystal structure of CRP-(cAMP)(2), which is evidence that the cAMP binding mode does not differ between the two complexes. Cyclic AMP 44-48 C-reactive protein Homo sapiens 39-42 11979597-3 2002 The Raman spectra of CRP-(cAMP)(1) and CRP-(cAMP)(2) extracted from those of CRP-cAMP mixtures at varied mixing ratios clearly show that the hydrogen bonding state and the conformation of cAMP in both complexes in solution are very similar to those found in the X-ray crystal structure of CRP-(cAMP)(2), which is evidence that the cAMP binding mode does not differ between the two complexes. Cyclic AMP 44-48 C-reactive protein Homo sapiens 39-42 11979597-3 2002 The Raman spectra of CRP-(cAMP)(1) and CRP-(cAMP)(2) extracted from those of CRP-cAMP mixtures at varied mixing ratios clearly show that the hydrogen bonding state and the conformation of cAMP in both complexes in solution are very similar to those found in the X-ray crystal structure of CRP-(cAMP)(2), which is evidence that the cAMP binding mode does not differ between the two complexes. Cyclic AMP 44-48 C-reactive protein Homo sapiens 39-42 11979597-3 2002 The Raman spectra of CRP-(cAMP)(1) and CRP-(cAMP)(2) extracted from those of CRP-cAMP mixtures at varied mixing ratios clearly show that the hydrogen bonding state and the conformation of cAMP in both complexes in solution are very similar to those found in the X-ray crystal structure of CRP-(cAMP)(2), which is evidence that the cAMP binding mode does not differ between the two complexes. Cyclic AMP 44-48 C-reactive protein Homo sapiens 39-42 11979597-3 2002 The Raman spectra of CRP-(cAMP)(1) and CRP-(cAMP)(2) extracted from those of CRP-cAMP mixtures at varied mixing ratios clearly show that the hydrogen bonding state and the conformation of cAMP in both complexes in solution are very similar to those found in the X-ray crystal structure of CRP-(cAMP)(2), which is evidence that the cAMP binding mode does not differ between the two complexes. Cyclic AMP 44-48 C-reactive protein Homo sapiens 39-42 11979597-3 2002 The Raman spectra of CRP-(cAMP)(1) and CRP-(cAMP)(2) extracted from those of CRP-cAMP mixtures at varied mixing ratios clearly show that the hydrogen bonding state and the conformation of cAMP in both complexes in solution are very similar to those found in the X-ray crystal structure of CRP-(cAMP)(2), which is evidence that the cAMP binding mode does not differ between the two complexes. Cyclic AMP 44-48 C-reactive protein Homo sapiens 39-42 11979597-3 2002 The Raman spectra of CRP-(cAMP)(1) and CRP-(cAMP)(2) extracted from those of CRP-cAMP mixtures at varied mixing ratios clearly show that the hydrogen bonding state and the conformation of cAMP in both complexes in solution are very similar to those found in the X-ray crystal structure of CRP-(cAMP)(2), which is evidence that the cAMP binding mode does not differ between the two complexes. Cyclic AMP 44-48 C-reactive protein Homo sapiens 39-42 11979597-3 2002 The Raman spectra of CRP-(cAMP)(1) and CRP-(cAMP)(2) extracted from those of CRP-cAMP mixtures at varied mixing ratios clearly show that the hydrogen bonding state and the conformation of cAMP in both complexes in solution are very similar to those found in the X-ray crystal structure of CRP-(cAMP)(2), which is evidence that the cAMP binding mode does not differ between the two complexes. Cyclic AMP 44-48 C-reactive protein Homo sapiens 39-42 11979597-3 2002 The Raman spectra of CRP-(cAMP)(1) and CRP-(cAMP)(2) extracted from those of CRP-cAMP mixtures at varied mixing ratios clearly show that the hydrogen bonding state and the conformation of cAMP in both complexes in solution are very similar to those found in the X-ray crystal structure of CRP-(cAMP)(2), which is evidence that the cAMP binding mode does not differ between the two complexes. Cyclic AMP 44-48 C-reactive protein Homo sapiens 39-42 11979597-3 2002 The Raman spectra of CRP-(cAMP)(1) and CRP-(cAMP)(2) extracted from those of CRP-cAMP mixtures at varied mixing ratios clearly show that the hydrogen bonding state and the conformation of cAMP in both complexes in solution are very similar to those found in the X-ray crystal structure of CRP-(cAMP)(2), which is evidence that the cAMP binding mode does not differ between the two complexes. Cyclic AMP 44-48 C-reactive protein Homo sapiens 39-42 11979597-3 2002 The Raman spectra of CRP-(cAMP)(1) and CRP-(cAMP)(2) extracted from those of CRP-cAMP mixtures at varied mixing ratios clearly show that the hydrogen bonding state and the conformation of cAMP in both complexes in solution are very similar to those found in the X-ray crystal structure of CRP-(cAMP)(2), which is evidence that the cAMP binding mode does not differ between the two complexes. Cyclic AMP 44-48 C-reactive protein Homo sapiens 39-42 11979597-3 2002 The Raman spectra of CRP-(cAMP)(1) and CRP-(cAMP)(2) extracted from those of CRP-cAMP mixtures at varied mixing ratios clearly show that the hydrogen bonding state and the conformation of cAMP in both complexes in solution are very similar to those found in the X-ray crystal structure of CRP-(cAMP)(2), which is evidence that the cAMP binding mode does not differ between the two complexes. Cyclic AMP 44-48 C-reactive protein Homo sapiens 39-42 11979597-3 2002 The Raman spectra of CRP-(cAMP)(1) and CRP-(cAMP)(2) extracted from those of CRP-cAMP mixtures at varied mixing ratios clearly show that the hydrogen bonding state and the conformation of cAMP in both complexes in solution are very similar to those found in the X-ray crystal structure of CRP-(cAMP)(2), which is evidence that the cAMP binding mode does not differ between the two complexes. Cyclic AMP 44-48 C-reactive protein Homo sapiens 39-42 11979597-3 2002 The Raman spectra of CRP-(cAMP)(1) and CRP-(cAMP)(2) extracted from those of CRP-cAMP mixtures at varied mixing ratios clearly show that the hydrogen bonding state and the conformation of cAMP in both complexes in solution are very similar to those found in the X-ray crystal structure of CRP-(cAMP)(2), which is evidence that the cAMP binding mode does not differ between the two complexes. Cyclic AMP 44-48 C-reactive protein Homo sapiens 39-42 11979597-3 2002 The Raman spectra of CRP-(cAMP)(1) and CRP-(cAMP)(2) extracted from those of CRP-cAMP mixtures at varied mixing ratios clearly show that the hydrogen bonding state and the conformation of cAMP in both complexes in solution are very similar to those found in the X-ray crystal structure of CRP-(cAMP)(2), which is evidence that the cAMP binding mode does not differ between the two complexes. Cyclic AMP 44-48 C-reactive protein Homo sapiens 39-42 11979597-5 2002 The environmental change of Trp85 suggests an opening of the cleft between the N-terminal cAMP and C-terminal DNA binding domains in the process of CRP activation by binding of a single cAMP molecule. Cyclic AMP 90-94 C-reactive protein Homo sapiens 148-151 11979597-5 2002 The environmental change of Trp85 suggests an opening of the cleft between the N-terminal cAMP and C-terminal DNA binding domains in the process of CRP activation by binding of a single cAMP molecule. Cyclic AMP 186-190 C-reactive protein Homo sapiens 148-151 11591152-2 2001 Analysis of amino acid residue proximity to cAMP in molecular dynamics (MD) simulations of the CRP:(cAMP)(2) complex [Garcia, A. E., and Harman, J. G. (1996) Protein Sci. Cyclic AMP 44-48 C-reactive protein Homo sapiens 95-98 11591152-2 2001 Analysis of amino acid residue proximity to cAMP in molecular dynamics (MD) simulations of the CRP:(cAMP)(2) complex [Garcia, A. E., and Harman, J. G. (1996) Protein Sci. Cyclic AMP 100-104 C-reactive protein Homo sapiens 95-98 11591152-4 2001 To test the role of Y99 in cAMP-mediated CRP activation, Y99 was substituted with alanine (A) or phenylalanine (F). Cyclic AMP 27-31 C-reactive protein Homo sapiens 41-44 11591152-5 2001 Cells that contained the WT or mutant forms of CRP induced beta-galactosidase in the presence of cAMP. Cyclic AMP 97-101 C-reactive protein Homo sapiens 47-50 11591152-6 2001 Purified WT, Y99A, and Y99F CRP showed only a 3- to 4-fold difference in cAMP affinity. Cyclic AMP 73-77 C-reactive protein Homo sapiens 28-31 11591152-9 2001 Whereas the WT or Y99F CRP:(cAMP)(1) complexes were cleaved by protease at hinge-region peptide bonds, the Y99A CRP:(cAMP)(1) complex was cleaved at peptide bonds located at the subunit interface. Cyclic AMP 28-32 C-reactive protein Homo sapiens 23-26 11591152-9 2001 Whereas the WT or Y99F CRP:(cAMP)(1) complexes were cleaved by protease at hinge-region peptide bonds, the Y99A CRP:(cAMP)(1) complex was cleaved at peptide bonds located at the subunit interface. Cyclic AMP 117-121 C-reactive protein Homo sapiens 112-115 11591152-10 2001 The rates of subunit exchange for Y99A CRP, both in the apo-form and in a 1:1 complex with cAMP, were significantly greater than that measured for WT CRP. Cyclic AMP 91-95 C-reactive protein Homo sapiens 39-42 11432780-2 2001 Upon the binding of cyclic AMP, CRP is allosterically activated, binds to target DNA sites, and interacts with RNA polymerase. Cyclic AMP 20-30 C-reactive protein Homo sapiens 32-35 11432780-5 2001 The result of (13)C-carbonyl NMR experiment on [(13)C"-Met]-CRP in the presence of both cyclic AMP and RNA polymerase alpha subunit showed that the two proteins interact with each other in solution in the absence of DNA via the region around the residues from Met 157 to Met 163 in CRP. Cyclic AMP 88-98 C-reactive protein Homo sapiens 60-63 11432780-5 2001 The result of (13)C-carbonyl NMR experiment on [(13)C"-Met]-CRP in the presence of both cyclic AMP and RNA polymerase alpha subunit showed that the two proteins interact with each other in solution in the absence of DNA via the region around the residues from Met 157 to Met 163 in CRP. Cyclic AMP 88-98 C-reactive protein Homo sapiens 282-285 11124966-1 2001 The x-ray crystal structure of the cAMP-ligated T127L/S128A double mutant of cAMP receptor protein (CRP) was determined to a resolution of 2.2 A. Cyclic AMP 35-39 C-reactive protein Homo sapiens 100-103 11124966-1 2001 The x-ray crystal structure of the cAMP-ligated T127L/S128A double mutant of cAMP receptor protein (CRP) was determined to a resolution of 2.2 A. Cyclic AMP 77-81 C-reactive protein Homo sapiens 100-103 11124966-2 2001 Although this structure is close to that of the x-ray crystal structure of cAMP-ligated CRP with one subunit in the open form and one subunit in the closed form, a bound syn-cAMP is clearly observed in the closed subunit in a third binding site in the C-terminal domain. Cyclic AMP 75-79 C-reactive protein Homo sapiens 88-91 11124966-2 2001 Although this structure is close to that of the x-ray crystal structure of cAMP-ligated CRP with one subunit in the open form and one subunit in the closed form, a bound syn-cAMP is clearly observed in the closed subunit in a third binding site in the C-terminal domain. Cyclic AMP 174-178 C-reactive protein Homo sapiens 88-91 11124966-3 2001 In addition, water-mediated interactions replace the hydrogen bonding interactions between the N(6) of anti-cAMP bound in the N-terminal domains of each subunit and the OH groups of the Thr(127) and Ser(128) residues in the C alpha-helix of wild type CRP. Cyclic AMP 108-112 C-reactive protein Homo sapiens 251-254 11124966-4 2001 This replacement induces flexibility in the C alpha-helix at Ala(128), which swings the C-terminal domain of the open subunit more toward the N-terminal domain in the T127L/S128A double mutant of CRP (CRP*) than is observed in the open subunit of cAMP-ligated CRP. Cyclic AMP 247-251 C-reactive protein Homo sapiens 196-199 11124966-4 2001 This replacement induces flexibility in the C alpha-helix at Ala(128), which swings the C-terminal domain of the open subunit more toward the N-terminal domain in the T127L/S128A double mutant of CRP (CRP*) than is observed in the open subunit of cAMP-ligated CRP. Cyclic AMP 247-251 C-reactive protein Homo sapiens 201-205 11124966-4 2001 This replacement induces flexibility in the C alpha-helix at Ala(128), which swings the C-terminal domain of the open subunit more toward the N-terminal domain in the T127L/S128A double mutant of CRP (CRP*) than is observed in the open subunit of cAMP-ligated CRP. Cyclic AMP 247-251 C-reactive protein Homo sapiens 201-204 11124966-5 2001 Isothermal titration calorimetry measurements on the binding of cAMP to CRP* show that the binding mechanism changes from an exothermic independent two-site binding mechanism at pH 7.0 to an endothermic interacting two-site mechanism at pH 5.2, similar to that observed for CRP at both pH levels. Cyclic AMP 64-68 C-reactive protein Homo sapiens 72-76 11124966-5 2001 Isothermal titration calorimetry measurements on the binding of cAMP to CRP* show that the binding mechanism changes from an exothermic independent two-site binding mechanism at pH 7.0 to an endothermic interacting two-site mechanism at pH 5.2, similar to that observed for CRP at both pH levels. Cyclic AMP 64-68 C-reactive protein Homo sapiens 72-75 11124966-7 2001 These properties and the bound syn-cAMP ligand, which has only been previously observed in the DNA bound x-ray crystal structure of cAMP-ligated CRP by Passner and Steitz (Passner, J. M., and Steitz, T. A. Cyclic AMP 35-39 C-reactive protein Homo sapiens 145-148 11124966-7 2001 These properties and the bound syn-cAMP ligand, which has only been previously observed in the DNA bound x-ray crystal structure of cAMP-ligated CRP by Passner and Steitz (Passner, J. M., and Steitz, T. A. Cyclic AMP 132-136 C-reactive protein Homo sapiens 145-148 10934201-2 2000 The cNMP-ligated CRP and mutants were cAMP, cGMP, and cIMP ligated with CRP, T127L CRP, S128A CRP, and T127L/S128A CRP. Cyclic AMP 38-42 C-reactive protein Homo sapiens 17-20 10934201-3 2000 The transcriptional activation of a 152-base pair lacUV5 promoter (synlac promoter) with a CRP consensus binding site sequence (syncon promoter) was enhanced by an average factor of 12.3 +/- 0.5 with the cAMP-ligated complexes of CRP/mutants and cGMP-ligated T127L, although their promoter binding site affinities varied by a factor of 5. Cyclic AMP 204-208 C-reactive protein Homo sapiens 91-94 10934201-3 2000 The transcriptional activation of a 152-base pair lacUV5 promoter (synlac promoter) with a CRP consensus binding site sequence (syncon promoter) was enhanced by an average factor of 12.3 +/- 0.5 with the cAMP-ligated complexes of CRP/mutants and cGMP-ligated T127L, although their promoter binding site affinities varied by a factor of 5. Cyclic AMP 204-208 C-reactive protein Homo sapiens 230-233 10934201-4 2000 However, in the presence of bound RNA polymerase, the binding affinities only ranged from 0.8 +/- 0.2 x 10(7) m(-)(1) for cAMP-ligated CRP* to 1.8 +/- 0. Cyclic AMP 122-126 C-reactive protein Homo sapiens 135-138 10934201-5 2000 3 x 10(7) m(-)(1) for cAMP-ligated CRP, indicating that the CRP/mutant interacts with the bound RNA polymerase, which would account for the near constancy of the enhancement factors. Cyclic AMP 22-26 C-reactive protein Homo sapiens 35-38 10934201-5 2000 3 x 10(7) m(-)(1) for cAMP-ligated CRP, indicating that the CRP/mutant interacts with the bound RNA polymerase, which would account for the near constancy of the enhancement factors. Cyclic AMP 22-26 C-reactive protein Homo sapiens 60-63 8702903-0 1996 Effect of cAMP binding site mutations on the interaction of cAMP receptor protein with cyclic nucleoside monophosphate ligands and DNA. Cyclic AMP 10-14 C-reactive protein Homo sapiens 60-81 10066748-5 1999 The reduction of the binding constants with increase in KCl concentration indicated the formation of two ion pairs for the cAMP-ligated CRP and S128A complexes and four ion pairs for the cAMP-ligated T127L and CRP* complexes. Cyclic AMP 123-127 C-reactive protein Homo sapiens 136-139 10066748-5 1999 The reduction of the binding constants with increase in KCl concentration indicated the formation of two ion pairs for the cAMP-ligated CRP and S128A complexes and four ion pairs for the cAMP-ligated T127L and CRP* complexes. Cyclic AMP 187-191 C-reactive protein Homo sapiens 210-213 10066748-7 1999 Small angle neutron scattering measurements on the lacDNA.CRP(cAMP)2 complex in D2O/H2O mixtures show that the DNA is bent around the cAMP-ligated protein in solution. Cyclic AMP 62-66 C-reactive protein Homo sapiens 58-61 9451003-5 1998 When the CRP-binding sites are deleted, CRP still interacts in a cAMP-dependent manner with the stable Esigma54 closed complex via protein-protein contacts. Cyclic AMP 65-69 C-reactive protein Homo sapiens 9-12 9451003-5 1998 When the CRP-binding sites are deleted, CRP still interacts in a cAMP-dependent manner with the stable Esigma54 closed complex via protein-protein contacts. Cyclic AMP 65-69 C-reactive protein Homo sapiens 40-43 9451003-11 1998 Thus, Esigma54 promoters are responsive to CRP, a protein unrelated to sigma54 activators, and the repression exerted is the direct result of an interaction between Esigma54 and the CRP-cAMP complex. Cyclic AMP 186-190 C-reactive protein Homo sapiens 43-46 9451003-11 1998 Thus, Esigma54 promoters are responsive to CRP, a protein unrelated to sigma54 activators, and the repression exerted is the direct result of an interaction between Esigma54 and the CRP-cAMP complex. Cyclic AMP 186-190 C-reactive protein Homo sapiens 182-185 9283073-8 1997 The F alpha-helix, which provides all base-specific contacts in the CRP-DNA complex, became hypersensitive to Fe-EDTA-mediated cleavage, whereas the solvent exposure of D and E alpha-helices was decreased upon binding of cAMP. Cyclic AMP 221-225 C-reactive protein Homo sapiens 68-71 9283073-9 1997 These results suggest that a significant part of cAMP-induced conformational change in CRP involves a movement of secondary structure elements in the C-terminal domain of the protein so that the recognition F alpha-helix becomes exposed to the solvent. Cyclic AMP 49-53 C-reactive protein Homo sapiens 87-90 10066748-3 1999 The binding reactions of the DNA duplexes to the fully cNMP-ligated CRP-mutant complexes were endothermic with binding constants as high as 6.6 +/- 1.1 x 10(6) M-1 (conDNA.CRP(cAMP)2). Cyclic AMP 176-180 C-reactive protein Homo sapiens 68-71 10066748-3 1999 The binding reactions of the DNA duplexes to the fully cNMP-ligated CRP-mutant complexes were endothermic with binding constants as high as 6.6 +/- 1.1 x 10(6) M-1 (conDNA.CRP(cAMP)2). Cyclic AMP 176-180 C-reactive protein Homo sapiens 172-175 10066748-4 1999 ConDNA binding to the unligated T127L and CRP* mutants was observed as well as conDNA and lacDNA binding to CRP with cAMP bound to only one monomer. Cyclic AMP 117-121 C-reactive protein Homo sapiens 108-111 9685337-4 1998 Thus, it appears that CRP undergoes a conformational change from the open form to the closed form in solution upon ligation with cAMP. Cyclic AMP 129-133 C-reactive protein Homo sapiens 22-25 9685337-5 1998 The SANS data from the CRP* and cAMP-ligated CRP* are coincidental, which implies that there is very little structural difference between the two species of CRP*. Cyclic AMP 32-36 C-reactive protein Homo sapiens 45-49 9685337-5 1998 The SANS data from the CRP* and cAMP-ligated CRP* are coincidental, which implies that there is very little structural difference between the two species of CRP*. Cyclic AMP 32-36 C-reactive protein Homo sapiens 45-49 9685337-6 1998 This is in agreement with in vivo results, which show that whereas CRP activates transcription in the cell only in the presence of cAMP, CRP* activates transcription in the absence of cAMP, implying that CRP* is already in the correct conformation for the activation of transcription. Cyclic AMP 131-135 C-reactive protein Homo sapiens 67-70 9283073-0 1997 Mapping conformational changes in a protein: application of a protein footprinting technique to cAMP-induced conformational changes in cAMP receptor protein. Cyclic AMP 96-100 C-reactive protein Homo sapiens 135-156 9283073-2 1997 The binding of cAMP to CRP dramatically increases the specific DNA binding activity of the protein and, as has been previously shown, induces conformational changes in the protein. Cyclic AMP 15-19 C-reactive protein Homo sapiens 23-26 9283073-4 1997 Binding of cAMP produced measurable differences in the susceptibility of CRP to the cleavage by Fe-EDTA. Cyclic AMP 11-15 C-reactive protein Homo sapiens 73-76 9264036-0 1997 CRP:cAMP complex binding to the lac operator region induces a structural change in lac DNA. Cyclic AMP 4-8 C-reactive protein Homo sapiens 0-3 9264036-3 1997 At CRP:cAMP complex concentrations greater than 200 nM, decreases in jM correlated with CRP binding to both the promoter-proximal and the operator-proximal CRP binding sites. Cyclic AMP 7-11 C-reactive protein Homo sapiens 3-6 9264036-3 1997 At CRP:cAMP complex concentrations greater than 200 nM, decreases in jM correlated with CRP binding to both the promoter-proximal and the operator-proximal CRP binding sites. Cyclic AMP 7-11 C-reactive protein Homo sapiens 88-91 9264036-3 1997 At CRP:cAMP complex concentrations greater than 200 nM, decreases in jM correlated with CRP binding to both the promoter-proximal and the operator-proximal CRP binding sites. Cyclic AMP 7-11 C-reactive protein Homo sapiens 88-91 9264036-4 1997 These results show that binding of the CRP:cAMP complex to the operator-proximal CRP binding site induces a structural change in lac DNA. Cyclic AMP 43-47 C-reactive protein Homo sapiens 39-42 9264036-4 1997 These results show that binding of the CRP:cAMP complex to the operator-proximal CRP binding site induces a structural change in lac DNA. Cyclic AMP 43-47 C-reactive protein Homo sapiens 81-84 8702903-1 1996 Although cAMP binding to wild type cAMP receptor protein (CRP) induces specific DNA binding and activates transcription, cyclic nucleoside monophosphate (cNMP) binding to the CRP mutant Ser128 --> Ala does not, whereas the double CRP mutant Thr127 --> Leu/Ser128 --> Ala activates transcription even in the absence of cNMP. Cyclic AMP 9-13 C-reactive protein Homo sapiens 35-56 8702903-1 1996 Although cAMP binding to wild type cAMP receptor protein (CRP) induces specific DNA binding and activates transcription, cyclic nucleoside monophosphate (cNMP) binding to the CRP mutant Ser128 --> Ala does not, whereas the double CRP mutant Thr127 --> Leu/Ser128 --> Ala activates transcription even in the absence of cNMP. Cyclic AMP 9-13 C-reactive protein Homo sapiens 58-61 8702903-2 1996 Isothermal titration calorimetry measurements on the cNMP binding reactions to the S128A and T127L/S128A mutants show that the reactions are mainly entropically driven as is cAMP binding to CRP. Cyclic AMP 174-178 C-reactive protein Homo sapiens 190-193 8702903-3 1996 In contrast to cAMP binding to CRP, the binding reactions are noncooperative and exothermic with binding enthalpies (DeltaHb) ranging from -23.4 +/- 0.9 kJ mol-1 for cAMP binding to S128A at 39 degrees C to -4.1 +/- 0.6 kJ mol-1 for cAMP binding to T127L/S128A at 24 degrees C and exhibit enthalpy-entropy compensation. Cyclic AMP 15-19 C-reactive protein Homo sapiens 31-34 8702903-5 1996 The cAMP-ligated S128A mutant binds to the consensus DNA binding site with approximately the same affinity as that of cAMP-ligated CRP but forms a different type of complex, which may account for loss of transcriptional activity by the mutant. Cyclic AMP 4-8 C-reactive protein Homo sapiens 131-134 8702903-5 1996 The cAMP-ligated S128A mutant binds to the consensus DNA binding site with approximately the same affinity as that of cAMP-ligated CRP but forms a different type of complex, which may account for loss of transcriptional activity by the mutant. Cyclic AMP 118-122 C-reactive protein Homo sapiens 131-134 8702903-6 1996 Energy minimization computations on the cAMP-ligated S128A mutant show that amino acid conformational differences between S128A and CRP occur at Ser179, Glu181, and Thr182 in the center of the DNA binding site, implying that these conformational changes may account for the difference in DNA binding. Cyclic AMP 40-44 C-reactive protein Homo sapiens 132-135 1645189-0 1991 Comparison of cAMP receptor protein (CRP) and a cAMP-independent form of CRP by Raman spectroscopy and DNA binding. Cyclic AMP 14-18 C-reactive protein Homo sapiens 37-40 7665583-2 1995 In contrast, the overall binding of cGMP to CRP is exothermic and non-cooperative with delta Hb, delta Cp, and delta Sb values close to the those values for binding of the first cAMP molecule to CRP. Cyclic AMP 178-182 C-reactive protein Homo sapiens 44-47 7665583-2 1995 In contrast, the overall binding of cGMP to CRP is exothermic and non-cooperative with delta Hb, delta Cp, and delta Sb values close to the those values for binding of the first cAMP molecule to CRP. Cyclic AMP 178-182 C-reactive protein Homo sapiens 195-198 1645189-4 1991 Raman analysis indicates that CRP structural changes induced by one bound cAMP or by the Gly to Gln mutation at residue 141 are small. Cyclic AMP 74-78 C-reactive protein Homo sapiens 30-33 8312976-7 1993 The CRP derivative is shown to retain 100% of the native protein cAMP binding and specific DNA binding activity. Cyclic AMP 65-69 C-reactive protein Homo sapiens 4-7 2162197-2 1990 Spectra were obtained over the range 400-1900 cm-1 from solutions of CRP and from CRP-cAMP cocrystals. Cyclic AMP 86-90 C-reactive protein Homo sapiens 82-85 1645189-11 1991 CRP*141 gln exhibited the same conformational characteristics of previously reported cAMP-independent mutant proteins. Cyclic AMP 85-89 C-reactive protein Homo sapiens 0-3 2162197-7 1990 Raman spectra of CRP-cAMP cocrystals differed from the spectra of CRP in solution. Cyclic AMP 21-25 C-reactive protein Homo sapiens 17-20 2162197-10 1990 Analysis of the amide I region of the CRP-cAMP cocrystal spectrum indicated a secondary structure distribution of 37% alpha-helix, 33% beta-strand, 17% turn, and 12% undefined. Cyclic AMP 42-46 C-reactive protein Homo sapiens 38-41 2162197-11 1990 This result is in agreement with a published secondary structure distribution derived from X-ray analysis of CRP-cAMP cocrystals (37% alpha-helix and 36% beta-strand). Cyclic AMP 113-117 C-reactive protein Homo sapiens 109-112 2163402-0 1990 A nuclear magnetic resonance study of the cyclic AMP receptor protein (CRP): assignments of the NH protons of histidine and tryptophan residues and the effect of binding of cAMP to CRP. Cyclic AMP 173-177 C-reactive protein Homo sapiens 42-69 2163402-0 1990 A nuclear magnetic resonance study of the cyclic AMP receptor protein (CRP): assignments of the NH protons of histidine and tryptophan residues and the effect of binding of cAMP to CRP. Cyclic AMP 173-177 C-reactive protein Homo sapiens 71-74 2163402-0 1990 A nuclear magnetic resonance study of the cyclic AMP receptor protein (CRP): assignments of the NH protons of histidine and tryptophan residues and the effect of binding of cAMP to CRP. Cyclic AMP 173-177 C-reactive protein Homo sapiens 181-184 2163402-5 1990 On the addition of cAMP and cGMP, signals F and G shifted up- and downfield respectively and conformational changes in the structure of CRP could be detected. Cyclic AMP 19-23 C-reactive protein Homo sapiens 136-139 34659176-8 2021 The cAMP receptor protein (CRP) is a major transcriptional regulator in bacteria that plays a key role in metabolic regulation. Cyclic AMP 4-8 C-reactive protein Homo sapiens 27-30